HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70.
Protein type: Chaperone; Heat shock protein; Motility/polarity/chemotaxis
Cellular Component: signalosome; focal adhesion; protein complex; mitochondrion; basolateral plasma membrane; inclusion body; cytosol; ribonucleoprotein complex; centriole; perinuclear region of cytoplasm; apical plasma membrane; cytoplasm; nuclear speck; intracellular; nucleus; ubiquitin ligase complex; vesicle
Molecular Function: protease binding; ATPase activity; unfolded protein binding; protein N-terminus binding; NF-kappaB binding; protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; double-stranded RNA binding; ATPase activity, coupled; ATP binding
Biological Process: binding of sperm to zona pellucida; positive regulation of T cell mediated cytotoxicity; positive regulation of erythrocyte differentiation; defense response; negative regulation of caspase activity; response to unfolded protein; negative regulation of vasoconstriction; negative regulation of cell proliferation; negative regulation of myeloid cell apoptosis; response to heat; mRNA catabolic process; protein refolding; negative regulation of protein ubiquitination; negative regulation of cell growth; negative regulation of apoptosis
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